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Protein

Vascular endothelial growth factor A

Gene

VEGFA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Growth factor active in angiogenesis, vasculogenesis and endothelial cell growth. Induces endothelial cell proliferation, promotes cell migration, inhibits apoptosis and induces permeabilization of blood vessels. Binds to the FLT1/VEGFR1 and KDR/VEGFR2 receptors, heparan sulfate and heparin. NRP1/Neuropilin-1 binds isoforms VEGF-165 and VEGF-145. Isoform VEGF165B binds to KDR but does not activate downstream signaling pathways, does not activate angiogenesis and inhibits tumor growth. Binding to NRP1 receptor initiates a signaling pathway needed for motor neuron axon guidance and cell body migration, including for the caudal migration of facial motor neurons from rhombomere 4 to rhombomere 6 during embryonic development (By similarity).By similarity2 Publications

GO - Molecular functioni

  • chemoattractant activity Source: UniProtKB
  • cytokine activity Source: BHF-UCL
  • extracellular matrix binding Source: BHF-UCL
  • fibronectin binding Source: BHF-UCL
  • growth factor activity Source: BHF-UCL
  • heparin binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • neuropilin binding Source: BHF-UCL
  • platelet-derived growth factor receptor binding Source: BHF-UCL
  • protein heterodimerization activity Source: MGI
  • protein homodimerization activity Source: BHF-UCL
  • receptor ligand activity Source: BHF-UCL
  • vascular endothelial growth factor receptor 1 binding Source: BHF-UCL
  • vascular endothelial growth factor receptor 2 binding Source: BHF-UCL
  • vascular endothelial growth factor receptor binding Source: UniProtKB

GO - Biological processi

  • activation of protein kinase activity Source: BHF-UCL
  • angiogenesis Source: UniProtKB
  • artery morphogenesis Source: BHF-UCL
  • basophil chemotaxis Source: UniProtKB
  • branching involved in blood vessel morphogenesis Source: BHF-UCL
  • branching morphogenesis of an epithelial tube Source: BHF-UCL
  • camera-type eye morphogenesis Source: BHF-UCL
  • cardiac muscle fiber development Source: BHF-UCL
  • cardiac vascular smooth muscle cell development Source: BHF-UCL
  • cell maturation Source: BHF-UCL
  • cell migration involved in sprouting angiogenesis Source: BHF-UCL
  • cellular response to hypoxia Source: MGI
  • cellular response to vascular endothelial growth factor stimulus Source: BHF-UCL
  • cellular stress response to acid chemical Source: BHF-UCL
  • commissural neuron axon guidance Source: BHF-UCL
  • coronary artery morphogenesis Source: BHF-UCL
  • coronary vein morphogenesis Source: BHF-UCL
  • cytokine-mediated signaling pathway Source: Reactome
  • dopaminergic neuron differentiation Source: BHF-UCL
  • endothelial cell chemotaxis Source: BHF-UCL
  • epithelial cell differentiation Source: BHF-UCL
  • eye photoreceptor cell development Source: BHF-UCL
  • growth Source: BHF-UCL
  • heart morphogenesis Source: BHF-UCL
  • induction of positive chemotaxis Source: UniProtKB
  • in utero embryonic development Source: BHF-UCL
  • kidney development Source: BHF-UCL
  • lactation Source: BHF-UCL
  • lung development Source: BHF-UCL
  • lymph vessel morphogenesis Source: BHF-UCL
  • macrophage differentiation Source: DFLAT
  • mammary gland alveolus development Source: BHF-UCL
  • mesoderm development Source: BHF-UCL
  • monocyte differentiation Source: DFLAT
  • motor neuron migration Source: UniProtKB
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  • negative regulation of gene expression Source: BHF-UCL
  • negative regulation of transcription by RNA polymerase II Source: BHF-UCL
  • nervous system development Source: UniProtKB
  • outflow tract morphogenesis Source: BHF-UCL
  • ovarian follicle development Source: BHF-UCL
  • platelet degranulation Source: Reactome
  • positive chemotaxis Source: BHF-UCL
  • positive regulation of angiogenesis Source: BHF-UCL
  • positive regulation of axon extension involved in axon guidance Source: BHF-UCL
  • positive regulation of blood vessel endothelial cell migration Source: BHF-UCL
  • positive regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis Source: BHF-UCL
  • positive regulation of branching involved in ureteric bud morphogenesis Source: BHF-UCL
  • positive regulation of cell adhesion Source: UniProtKB
  • positive regulation of cell division Source: UniProtKB-KW
  • positive regulation of cell migration Source: BHF-UCL
  • positive regulation of cell migration involved in sprouting angiogenesis Source: BHF-UCL
  • positive regulation of cell proliferation Source: BHF-UCL
  • positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway Source: BHF-UCL
  • positive regulation of cellular component movement Source: BHF-UCL
  • positive regulation of CREB transcription factor activity Source: BHF-UCL
  • positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway Source: BHF-UCL
  • positive regulation of endothelial cell migration Source: UniProtKB
  • positive regulation of endothelial cell proliferation Source: UniProtKB
  • positive regulation of epithelial cell proliferation Source: BHF-UCL
  • positive regulation of ERK1 and ERK2 cascade Source: BHF-UCL
  • positive regulation of focal adhesion assembly Source: UniProtKB
  • positive regulation of gene expression Source: BHF-UCL
  • positive regulation of histone deacetylase activity Source: BHF-UCL
  • positive regulation of leukocyte migration Source: BHF-UCL
  • positive regulation of MAP kinase activity Source: BHF-UCL
  • positive regulation of mast cell chemotaxis Source: UniProtKB
  • positive regulation of mesenchymal cell proliferation Source: BHF-UCL
  • positive regulation of neuroblast proliferation Source: BHF-UCL
  • positive regulation of p38MAPK cascade Source: UniProtKB
  • positive regulation of peptidyl-serine phosphorylation Source: BHF-UCL
  • positive regulation of peptidyl-tyrosine autophosphorylation Source: BHF-UCL
  • positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
  • positive regulation of phosphorylation Source: BHF-UCL
  • positive regulation of positive chemotaxis Source: BHF-UCL
  • positive regulation of protein autophosphorylation Source: BHF-UCL
  • positive regulation of protein complex assembly Source: UniProtKB
  • positive regulation of protein kinase C signaling Source: BHF-UCL
  • positive regulation of protein kinase D signaling Source: BHF-UCL
  • positive regulation of protein localization to early endosome Source: BHF-UCL
  • positive regulation of protein phosphorylation Source: UniProtKB
  • positive regulation of receptor internalization Source: BHF-UCL
  • positive regulation of retinal ganglion cell axon guidance Source: BHF-UCL
  • positive regulation of sprouting angiogenesis Source: BHF-UCL
  • positive regulation of transcription by RNA polymerase II Source: BHF-UCL
  • positive regulation of transcription from RNA polymerase II promoter in response to hypoxia Source: BHF-UCL
  • positive regulation of vascular endothelial growth factor receptor signaling pathway Source: BHF-UCL
  • positive regulation of vascular permeability Source: UniProtKB
  • post-embryonic camera-type eye development Source: BHF-UCL
  • primitive erythrocyte differentiation Source: BHF-UCL
  • regulation of cell shape Source: BHF-UCL
  • regulation of cGMP metabolic process Source: MGI
  • regulation of retinal ganglion cell axon guidance Source: BHF-UCL
  • regulation of transcription by RNA polymerase II Source: BHF-UCL
  • regulation of transcription from RNA polymerase II promoter in response to hypoxia Source: Reactome
  • response to hypoxia Source: UniProtKB
  • surfactant homeostasis Source: BHF-UCL
  • tube formation Source: UniProtKB
  • vascular endothelial growth factor receptor signaling pathway Source: BHF-UCL
  • vascular endothelial growth factor signaling pathway Source: BHF-UCL
  • vasculogenesis Source: UniProtKB
  • VEGF-activated neuropilin signaling pathway Source: BHF-UCL

Keywordsi

Molecular functionDevelopmental protein, Growth factor, Heparin-binding, Mitogen
Biological processAngiogenesis, Differentiation

Enzyme and pathway databases

ReactomeiR-HSA-114608 Platelet degranulation
R-HSA-1234158 Regulation of gene expression by Hypoxia-inducible Factor
R-HSA-194313 VEGF ligand-receptor interactions
R-HSA-195399 VEGF binds to VEGFR leading to receptor dimerization
R-HSA-4420097 VEGFA-VEGFR2 Pathway
R-HSA-5218921 VEGFR2 mediated cell proliferation
R-HSA-6785807 Interleukin-4 and 13 signaling
R-HSA-8866910 TFAP2 (AP-2) family regulates transcription of growth factors and their receptors
SIGNORiP15692

Names & Taxonomyi

Protein namesi
Recommended name:
Vascular endothelial growth factor A
Short name:
VEGF-A
Alternative name(s):
Vascular permeability factor
Short name:
VPF
Gene namesi
Name:VEGFA
Synonyms:VEGF
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

EuPathDBiHostDB:ENSG00000112715.20
HGNCiHGNC:12680 VEGFA
MIMi192240 gene
neXtProtiNX_P15692

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Microvascular complications of diabetes 1 (MVCD1)1 Publication
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionPathological conditions that develop in numerous tissues and organs as a consequence of diabetes mellitus. They include diabetic retinopathy, diabetic nephropathy leading to end-stage renal disease, and diabetic neuropathy. Diabetic retinopathy remains the major cause of new-onset blindness among diabetic adults. It is characterized by vascular permeability and increased tissue ischemia and angiogenesis.
See also OMIM:603933

Organism-specific databases

DisGeNETi7422
MalaCardsiVEGFA
MIMi603933 phenotype
OpenTargetsiENSG00000112715
PharmGKBiPA37302

Chemistry databases

ChEMBLiCHEMBL1783
DrugBankiDB05434 ABT-510
DB08885 Aflibercept
DB00112 Bevacizumab
DB01136 Carvedilol
DB06779 Dalteparin
DB01120 Gliclazide
DB01017 Minocycline
DB03088 Pyroglutamic Acid
DB01270 Ranibizumab
DB03754 Tris
DB05294 Vandetanib
DB05890 VEGF-AS

Polymorphism and mutation databases

BioMutaiVEGFA
DMDMi17380528

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 262 PublicationsAdd BLAST26
ChainiPRO_000002338627 – 232Vascular endothelial growth factor AAdd BLAST206

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi52 ↔ 94
Disulfide bondi77Interchain
Disulfide bondi83 ↔ 128
Disulfide bondi86Interchain
Disulfide bondi87 ↔ 130
Glycosylationi101N-linked (GlcNAc...) asparagine1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP15692
PeptideAtlasiP15692
PRIDEiP15692

PTM databases

iPTMnetiP15692
PhosphoSitePlusiP15692

Expressioni

Tissue specificityi

Isoform VEGF189, isoform VEGF165 and isoform VEGF121 are widely expressed. Isoform VEGF206 and isoform VEGF145 are not widely expressed. A higher level expression seen in pituitary tumors as compared to the pituitary gland.1 Publication

Inductioni

By hypoxia. Regulated by growth factors, cytokines, gonadotropins, nitric oxide, hypoglycemia and oncogenic mutations.1 Publication

Gene expression databases

BgeeiENSG00000112715
ExpressionAtlasiP15692 baseline and differential
GenevisibleiP15692 HS

Organism-specific databases

HPAiCAB005429
CAB039240
HPA069116

Interactioni

Subunit structurei

Homodimer; disulfide-linked. Also found as heterodimer with PGF (By similarity). Interacts with NRP1 (PubMed:26503042).By similarity1 Publication

Binary interactionsi

Show more details

GO - Molecular functioni

  • chemoattractant activity Source: UniProtKB
  • cytokine activity Source: BHF-UCL
  • fibronectin binding Source: BHF-UCL
  • growth factor activity Source: BHF-UCL
  • identical protein binding Source: IntAct
  • neuropilin binding Source: BHF-UCL
  • platelet-derived growth factor receptor binding Source: BHF-UCL
  • protein heterodimerization activity Source: MGI
  • protein homodimerization activity Source: BHF-UCL
  • receptor ligand activity Source: BHF-UCL
  • vascular endothelial growth factor receptor 1 binding Source: BHF-UCL
  • vascular endothelial growth factor receptor 2 binding Source: BHF-UCL
  • vascular endothelial growth factor receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi113265, 36 interactors
CORUMiP15692
DIPiDIP-5740N
IntActiP15692, 19 interactors
MINTiP15692
STRINGi9606.ENSP00000361125

Chemistry databases

BindingDBiP15692

Structurei

Secondary structure

1232
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi43 – 50Combined sources8
Beta strandi51 – 60Combined sources10
Helixi61 – 64Combined sources4
Helixi66 – 68Combined sources3
Beta strandi71 – 84Combined sources14
Beta strandi93 – 109Combined sources17
Turni111 – 113Combined sources3
Beta strandi116 – 131Combined sources16
Beta strandi189 – 191Combined sources3
Beta strandi194 – 197Combined sources4
Turni199 – 201Combined sources3
Beta strandi204 – 208Combined sources5
Helixi210 – 214Combined sources5
Turni215 – 217Combined sources3
Beta strandi219 – 221Combined sources3
Turni222 – 224Combined sources3
Beta strandi226 – 228Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BJ1X-ray2.40V/W34-135[»]
1CZ8X-ray2.40V/W40-133[»]
1FLTX-ray1.70V/W38-135[»]
1KATNMR-V/W37-135[»]
1KMXNMR-A183-232[»]
1MJVX-ray2.10A/B40-134[»]
1MKGX-ray2.50A/B/C/D40-134[»]
1MKKX-ray1.32A/B40-134[»]
1QTYX-ray2.70R/S/V/W34-135[»]
1TZHX-ray2.60V/W34-135[»]
1TZIX-ray2.80V34-135[»]
1VGHNMR-A180-232[»]
1VPFX-ray2.50A/B/C/D34-135[»]
1VPPX-ray1.90V/W34-135[»]
2FJGX-ray2.80V/W34-135[»]
2FJHX-ray3.10V/W34-135[»]
2QR0X-ray3.50C/D/I/J/O/P/U/V39-135[»]
2VGHNMR-A182-232[»]
2VPFX-ray1.93A/B/C/D/E/F/G/H34-135[»]
3BDYX-ray2.60V34-135[»]
3P9WX-ray2.41A/C/E/G35-138[»]
3QTKX-ray1.85A/B/C/D/E/F34-135[»]
3S1BX-ray2.90V38-133[»]
3S1KX-ray2.55V/W34-135[»]
3V2AX-ray3.20A27-140[»]
4DEQX-ray2.65A/B183-232[»]
4GLNX-ray1.60E/F34-135[»]
4GLSX-ray1.60E/F34-135[»]
4KZNX-ray1.71A39-135[»]
4QAFX-ray1.80C/D34-135[»]
4WPBX-ray3.11A/B34-135[»]
4ZFFX-ray2.75C/D37-135[»]
5DN2X-ray1.95E/F/G205-232[»]
5FV1X-ray2.70V/W27-136[»]
5FV2X-ray3.45V/W/X27-136[»]
5HHCX-ray2.10A/B34-135[»]
5HHDX-ray2.10A/B34-135[»]
5O4EX-ray2.15E/F39-134[»]
5T89X-ray4.00V/W27-155[»]
ProteinModelPortaliP15692
SMRiP15692
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15692

Family & Domainsi

Sequence similaritiesi

Belongs to the PDGF/VEGF growth factor family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IGCM Eukaryota
ENOG410ZWYU LUCA
GeneTreeiENSGT00730000110791
HOVERGENiHBG000105
InParanoidiP15692
KOiK05448
PhylomeDBiP15692

Family and domain databases

CDDicd00135 PDGF, 1 hit
Gene3Di2.10.160.10, 1 hit
2.10.90.10, 1 hit
InterProiView protein in InterPro
IPR029034 Cystine-knot_cytokine
IPR023581 PD_growth_factor_CS
IPR000072 PDGF/VEGF_dom
IPR027928 VEGF_C
IPR036841 VEGF_C_sf
PfamiView protein in Pfam
PF00341 PDGF, 1 hit
PF14554 VEGF_C, 1 hit
SMARTiView protein in SMART
SM00141 PDGF, 1 hit
SUPFAMiSSF57501 SSF57501, 1 hit
SSF57593 SSF57593, 1 hit
PROSITEiView protein in PROSITE
PS00249 PDGF_1, 1 hit
PS50278 PDGF_2, 1 hit

Sequences (17)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 17 isoformsi produced by alternative promoter usage, alternative splicing and alternative initiation. AlignAdd to basket

Note: Additional isoforms seem to exist.
Isoform VEGF206 (identifier: P15692-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MNFLLSWVHW SLALLLYLHH AKWSQAAPMA EGGGQNHHEV VKFMDVYQRS
60 70 80 90 100
YCHPIETLVD IFQEYPDEIE YIFKPSCVPL MRCGGCCNDE GLECVPTEES
110 120 130 140 150
NITMQIMRIK PHQGQHIGEM SFLQHNKCEC RPKKDRARQE KKSVRGKGKG
160 170 180 190 200
QKRKRKKSRY KSWSVYVGAR CCLMPWSLPG PHPCGPCSER RKHLFVQDPQ
210 220 230
TCKCSCKNTD SRCKARQLEL NERTCRCDKP RR
Length:232
Mass (Da):27,042
Last modified:November 16, 2001 - v2
Checksum:iFB49F364446F4D01
GO
Isoform VEGF189 (identifier: P15692-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     166-182: Missing.

Show »
Length:215
Mass (Da):25,173
Checksum:i7B9759AD5871FF33
GO
Isoform VEGF183 (identifier: P15692-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     160-182: Missing.

Show »
Length:209
Mass (Da):24,422
Checksum:iF01CCEACD945D6CA
GO
Isoform VEGF165 (identifier: P15692-4) [UniParc]FASTAAdd to basket
Also known as: VEGF

The sequence of this isoform differs from the canonical sequence as follows:
     141-141: K → N
     142-182: Missing.

Show »
Length:191
Mass (Da):22,314
Checksum:iCCE57097DD3779BD
GO
Isoform VEGF148 (identifier: P15692-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     141-141: K → N
     142-182: Missing.
     215-215: A → M
     216-232: Missing.

Show »
Length:174
Mass (Da):20,218
Checksum:iAE88400CA7757644
GO
Isoform VEGF145 (identifier: P15692-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     166-226: Missing.

Show »
Length:171
Mass (Da):20,064
Checksum:iD02ECA735FF6E9F8
GO
Isoform VEGF165B (identifier: P15692-8) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     141-141: K → N
     142-182: Missing.
     227-232: CDKPRR → SLTRKD

Show »
Length:191
Mass (Da):22,259
Checksum:iD25243E540AC79BD
GO
Isoform VEGF121 (identifier: P15692-9) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     142-226: Missing.

Note: No experimental confirmation available.
Show »
Length:147
Mass (Da):17,219
Checksum:iDDF4D6994249BED6
GO
Isoform VEGF111 (identifier: P15692-10) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     132-226: Missing.

Note: No experimental confirmation available.
Show »
Length:137
Mass (Da):15,981
Checksum:i196B2BB49381BE87
GO
Isoform L-VEGF165 (identifier: P15692-11) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MTDRQTDTAP...AGPGRASETM
     141-141: K → N
     142-182: Missing.

Note: Produced by alternative promoter usage and alternative initiation. Starts at an alternative upstream CUG codon. Post-translationally processed to produce the secreted VEGF peptide and a N-terminal peptide N-VEGF. The unprocessed protein and the N-VEGF peptide may localize to the nucleus (PubMed:15896327), the endoplasmic reticulum and the Golgi (PubMed:11731620) or the extracellular matrix (PubMed:11563986).3 Publications
Show »
Length:371
Mass (Da):40,738
Checksum:i053E9CA56725C07B
GO
Isoform L-VEGF121 (identifier: P15692-12) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MTDRQTDTAP...AGPGRASETM
     142-226: Missing.

Note: Produced by alternative promoter usage and alternative initiation. Starts at an alternative upstream CUG codon. Post-translationally processed to produce the secreted VEGF peptide and a N-terminal peptide N-VEGF. The unprocessed protein and the N-VEGF peptide may localize to the nucleus (PubMed:15896327), the endoplasmic reticulum and the Golgi (PubMed:11731620) or the extracellular matrix (PubMed:11563986).3 Publications
Show »
Length:327
Mass (Da):35,643
Checksum:i8D6F969601B2A9EF
GO
Isoform L-VEGF189 (identifier: P15692-13) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MTDRQTDTAP...AGPGRASETM
     166-182: Missing.

Note: Produced by alternative promoter usage and alternative initiation. Starts at an alternative upstream CUG codon. Post-translationally processed to produce the secreted VEGF peptide and a N-terminal peptide N-VEGF. The unprocessed protein and the N-VEGF peptide may localize to the nucleus (PubMed:15896327), the endoplasmic reticulum and the Golgi (PubMed:11731620) or the extracellular matrix (PubMed:11563986).3 Publications
Show »
Length:395
Mass (Da):43,597
Checksum:i8ADF6524B1835A2D
GO
Isoform L-VEGF206 (identifier: P15692-14) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MTDRQTDTAP...AGPGRASETM

Note: Gene prediction based on EST data. Produced by alternative promoter usage and alternative initiation. Starts at an alternative upstream CUG codon.
Show »
Length:412
Mass (Da):45,467
Checksum:iAC807D3F21528D35
GO
Isoform 15 (identifier: P15692-15) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MTDRQTDTAP...AGPGRASETM
     141-182: KKSVRGKGKGQKRKRKKSRYKSWSVYVGARCCLMPWSLPGPH → N
     227-232: CDKPRR → SLTRKD

Note: Starts at an alternative upstream CUG codon.
Show »
Length:371
Mass (Da):40,683
Checksum:i1B89AFD7FABEC07B
GO
Isoform 16 (identifier: P15692-16) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MTDRQTDTAP...AGPGRASETM
     160-182: Missing.

Note: Starts at an alternative upstream CUG codon.
Show »
Length:389
Mass (Da):42,846
Checksum:i950279CF7A273A0E
GO
Isoform 17 (identifier: P15692-17) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MTDRQTDTAP...AGPGRASETM
     141-182: KKSVRGKGKGQKRKRKKSRYKSWSVYVGARCCLMPWSLPGPH → N
     215-215: A → M
     216-232: Missing.

Note: Starts at an alternative upstream CUG codon.
Show »
Length:354
Mass (Da):38,642
Checksum:i0152409399BAB1EB
GO
Isoform 18 (identifier: P15692-18) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MTDRQTDTAP...AGPGRASETM
     132-226: Missing.

Note: Starts at an alternative upstream CUG codon.
Show »
Length:317
Mass (Da):34,406
Checksum:iFDF27C1251E3B613
GO

Sequence cautioni

The sequence AAC63102 differs from that shown. Reason: Erroneous initiation.Curated
The sequence AAC63143 differs from that shown. Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.Curated
The sequence CAC19512 differs from that shown. Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.Curated
The sequence CAC19516 differs from that shown. Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti87C → S in AAC63143 (PubMed:9450968).Curated1
Sequence conflicti210D → H in AAC63143 (PubMed:9450968).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0387451M → MTDRQTDTAPSPSYHLLPGR RRTVDAAASRGQGPEPAPGG GVEGVGARGVALKLFVQLLG CSRFGGAVVRAGEAEPSGAA RSASSGREEPQPEEGEEEEE KEEERGPQWRLGARKPGSWT GEAAVCADSAPAARAPQALA RASGRGGRVARRGAEESGPP HSPSRRGSASRAGPGRASET M in isoform L-VEGF165, isoform L-VEGF121, isoform L-VEGF189, isoform L-VEGF206, isoform 15, isoform 16, isoform 17 and isoform 18. 1 Publication1
Alternative sequenceiVSP_026781132 – 226Missing in isoform VEGF111 and isoform 18. 1 PublicationAdd BLAST95
Alternative sequenceiVSP_054111141 – 182KKSVR…LPGPH → N in isoform 15 and isoform 17. CuratedAdd BLAST42
Alternative sequenceiVSP_004618141K → N in isoform VEGF148, isoform VEGF165, isoform VEGF165B and isoform L-VEGF165. 10 Publications1
Alternative sequenceiVSP_004620142 – 226Missing in isoform VEGF121 and isoform L-VEGF121. 1 PublicationAdd BLAST85
Alternative sequenceiVSP_004619142 – 182Missing in isoform VEGF148, isoform VEGF165, isoform VEGF165B and isoform L-VEGF165. 10 PublicationsAdd BLAST41
Alternative sequenceiVSP_004621160 – 182Missing in isoform VEGF183 and isoform 16. 2 PublicationsAdd BLAST23
Alternative sequenceiVSP_004623166 – 226Missing in isoform VEGF145. 1 PublicationAdd BLAST61
Alternative sequenceiVSP_004622166 – 182Missing in isoform VEGF189 and isoform L-VEGF189. 2 PublicationsAdd BLAST17
Alternative sequenceiVSP_004624215A → M in isoform VEGF148 and isoform 17. 1 Publication1
Alternative sequenceiVSP_004625216 – 232Missing in isoform VEGF148 and isoform 17. 1 PublicationAdd BLAST17
Alternative sequenceiVSP_014783227 – 232CDKPRR → SLTRKD in isoform VEGF165B and isoform 15. 1 Publication6

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32977 mRNA Translation: AAA35789.1
M27281 mRNA Translation: AAA36807.1
M63978
, M63971, M63972, M63973, M63974, M63975, M63976, M63977 Genomic DNA Translation: AAA36804.1
S85192 mRNA Translation: AAC63102.1 Different initiation.
AH006909 Genomic DNA Translation: AAC63101.1
X62568 mRNA Translation: CAA44447.1
AJ010438 mRNA Translation: CAA09179.1
AF022375 mRNA Translation: AAC63143.1 Sequence problems.
AF091352 mRNA Translation: AAD55345.1
AF430806 mRNA Translation: AAL27435.1
AB021221 mRNA Translation: BAA78418.1
AF214570 mRNA Translation: AAF19659.1
AY047581 mRNA Translation: AAK95847.1
AF486837 mRNA Translation: AAM03108.1
AY766116 mRNA Translation: AAV34601.1
DQ229900 mRNA Translation: ABB58912.1
AB451322 mRNA Translation: BAG70136.1
AB451451 mRNA Translation: BAG70265.1
AL136131 Genomic DNA Translation: CAC19512.2 Sequence problems.
AL136131 Genomic DNA Translation: CAC19513.2
AL136131 Genomic DNA Translation: CAC19515.2
AL136131 Genomic DNA Translation: CAC19516.2 Sequence problems.
CH471081 Genomic DNA Translation: EAX04229.1
BC065522 mRNA Translation: AAH65522.2
AF437895 Genomic DNA Translation: AAL27630.1
AF062645 mRNA Translation: AAC16730.1
CCDSiCCDS34457.1 [P15692-14]
CCDS34458.1 [P15692-11]
CCDS47432.1 [P15692-15]
CCDS47433.1 [P15692-16]
CCDS47434.1 [P15692-12]
CCDS47435.1 [P15692-17]
CCDS4907.2 [P15692-13]
CCDS55007.1 [P15692-18]
CCDS55008.1 [P15692-3]
CCDS55009.1 [P15692-2]
CCDS55010.1 [P15692-1]
CCDS55011.1 [P15692-5]
CCDS55012.1 [P15692-4]
CCDS55013.1 [P15692-8]
CCDS55014.1 [P15692-9]
CCDS55015.1 [P15692-10]
PIRiA41551
RefSeqiNP_001020537.2, NM_001025366.2 [P15692-14]
NP_001020538.2, NM_001025367.2 [P15692-16]
NP_001020539.2, NM_001025368.2 [P15692-11]
NP_001020540.2, NM_001025369.2 [P15692-17]
NP_001020541.2, NM_001025370.2 [P15692-12]
NP_001028928.1, NM_001033756.2 [P15692-15]
NP_001165093.1, NM_001171622.1 [P15692-18]
NP_001165094.1, NM_001171623.1 [P15692-1]
NP_001165095.1, NM_001171624.1 [P15692-2]
NP_001165096.1, NM_001171625.1 [P15692-3]
NP_001165097.1, NM_001171626.1 [P15692-4]
NP_001165098.1, NM_001171627.1 [P15692-5]
NP_001165099.1, NM_001171628.1 [P15692-9]
NP_001165100.1, NM_001171629.1 [P15692-8]
NP_001165101.1, NM_001171630.1 [P15692-10]
NP_001191313.1, NM_001204384.1 [P15692-6]
NP_001191314.1, NM_001204385.1
NP_001273973.1, NM_001287044.1
NP_001303939.1, NM_001317010.1
NP_003367.4, NM_003376.5 [P15692-13]
UniGeneiHs.73793

Genome annotation databases

EnsembliENST00000372077; ENSP00000361148; ENSG00000112715 [P15692-9]
ENST00000457104; ENSP00000409911; ENSG00000112715 [P15692-10]
ENST00000518689; ENSP00000430829; ENSG00000112715 [P15692-3]
ENST00000518824; ENSP00000430002; ENSG00000112715 [P15692-8]
ENST00000520948; ENSP00000428321; ENSG00000112715 [P15692-2]
ENST00000523125; ENSP00000429008; ENSG00000112715 [P15692-5]
ENST00000523873; ENSP00000430479; ENSG00000112715 [P15692-1]
ENST00000523950; ENSP00000429643; ENSG00000112715 [P15692-4]
ENST00000611736; ENSP00000478570; ENSG00000112715 [P15692-14]
ENST00000615393; ENSP00000478034; ENSG00000112715 [P15692-12]
ENST00000617771; ENSP00000484284; ENSG00000112715 [P15692-15]
ENST00000621747; ENSP00000483241; ENSG00000112715 [P15692-11]
ENST00000640482; ENSP00000492800; ENSG00000112715 [P15692-17]
ENST00000640499; ENSP00000492413; ENSG00000112715 [P15692-13]
ENST00000640653; ENSP00000492199; ENSG00000112715 [P15692-16]
GeneIDi7422
KEGGihsa:7422
UCSCiuc003owd.5 human [P15692-1]

Keywords - Coding sequence diversityi

Alternative initiation, Alternative promoter usage, Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiVEGFA_HUMAN
AccessioniPrimary (citable) accession number: P15692
Secondary accession number(s): B5BU86
, H0Y2S8, H0Y407, H0Y414, H0Y462, H0Y8N2, H3BLW7, O60720, O75875, Q074Z4, Q16889, Q5UB46, Q6P0P5, Q96KJ0, Q96L82, Q96NW5, Q9H1W8, Q9H1W9, Q9UH58, Q9UL23
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: November 16, 2001
Last modified: April 25, 2018
This is version 230 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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